Evidence map›Paper›PMID 34737320›Full record

ArticleScientific reports2021

Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade.

Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka and 6 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
27.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Crowding in Anhydrobiosis.Sub-cellular biochemistry · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Transcriptome analysis of the tardigrade Hypsibius exemplaris exposed to the DNA-damaging agent bleomycin.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024
    Article
  18. Article
  19. Article
  20. Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 2 countries.

Maho Yagi-UtsumiExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Kazuhiro AokiExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Hiroki WatanabeExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Chihong SongExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Seiji NishimuraGraduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, 465-8603, Japan.
Tadashi SatohGraduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, 465-8603, Japan.
Saeko YanakaExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Christian GanserExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Sae TanakaExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Vincent SchnapkaInstitute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Aichi, 444-8787, Japan.
Ean Wai GohInstitute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Aichi, 444-8787, Japan.
Yuji FurutaniInstitute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Aichi, 444-8787, Japan.
Kazuyoshi MurataExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Takayuki UchihashiExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Kazuharu ArakawaExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
Koichi KatoExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan. kkato@excells.orion.ac.jp.
National Institutes of Natural Sciences · JPNagoya City University · JPKeio University · JPNational Institute for Physiological Sciences · JPNational Institute for Basic Biology · JP

Funding

Japan Science and Technology Agency JPMJCR17N5Japan Society for the Promotion of Science JP17H03620Japan Society for the Promotion of Science JP19K07041
6 · The paper itself

Abstract

Anhydrobiosis, one of the most extensively studied forms of cryptobiosis, is induced in certain organisms as a response to desiccation. Anhydrobiotic species has been hypothesized to produce substances that can protect their biological components and/or cell membranes without water. In extremotolerant tardigrades, highly hydrophilic and heat-soluble protein families, cytosolic abundant heat-soluble (CAHS) proteins, have been identified, which are postulated to be integral parts of the tardigrades' response to desiccation. In this study, to elucidate these protein functions, we performed in vitro and in vivo characterizations of the reversible self-assembling property of CAHS1 protein, a major isoform of CAHS proteins from Ramazzottius varieornatus, using a series of spectroscopic and microscopic techniques. We found that CAHS1 proteins homo-oligomerized via the C-terminal α-helical region and formed a hydrogel as their concentration increased. We also demonstrated that the overexpressed CAHS1 proteins formed condensates under desiccation-mimicking conditions. These data strongly suggested that, upon drying, the CAHS1 proteins form oligomers and eventually underwent sol-gel transition in tardigrade cytosols. Thus, it is proposed that the CAHS1 proteins form the cytosolic fibrous condensates, which presumably have variable mechanisms for the desiccation tolerance of tardigrades. These findings provide insights into molecular strategies of organisms to adapt to extreme environments.

Indexed as

DesiccationAdaptation, PhysiologicalAnimalsCytosolProteinsTardigradaProteins

Identifiers

PMID34737320
PMCPMC8569203
OpenAlexW3210960798

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.